Global profiling of distinct cysteine redox forms reveals wide-ranging redox regulation in C. elegans.

Nat Commun

State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing, China.

Published: March 2021

AI Article Synopsis

  • Post-translational modifications of cysteine residues can quickly change protein functions, influencing various biological processes.
  • C. elegans is an ideal model for examining these cysteine-mediated redox signaling at a network level.
  • The study offers a detailed analysis of the cysteine reactivity and redox changes in C. elegans, highlighting key events in translation, growth, and stress responses that are regulated by redox-sensitive cysteines, particularly within the p38 MAPK signaling pathway.

Article Abstract

Post-translational changes in the redox state of cysteine residues can rapidly and reversibly alter protein functions, thereby modulating biological processes. The nematode C. elegans is an ideal model organism for studying cysteine-mediated redox signaling at a network level. Here we present a comprehensive, quantitative, and site-specific profile of the intrinsic reactivity of the cysteinome in wild-type C. elegans. We also describe a global characterization of the C. elegans redoxome in which we measured changes in three major cysteine redox forms after HO treatment. Our data revealed redox-sensitive events in translation, growth signaling, and stress response pathways, and identified redox-regulated cysteines that are important for signaling through the p38 MAP kinase (MAPK) pathway. Our in-depth proteomic dataset provides a molecular basis for understanding redox signaling in vivo, and will serve as a valuable and rich resource for the field of redox biology.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7930113PMC
http://dx.doi.org/10.1038/s41467-021-21686-3DOI Listing

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